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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
chemical engineering
Enhancement of the thermostability of the maltogenic amylase MAUS149 by Gly312Ala and Lys436Arg substitutions
Bioresource Technology, Volume 102, No. 2, Year 2011
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Description
Based on sequence alignments and homology modeling, Gly 312 and Lys 436 of the maltogenic amylase from Bacillus sp. US149 (MAUS149) were selected as targets for site-directed mutagenesis to improve the thermostability of the enzyme. Variants of MAUS149 with amino acid substitutions G312A, K436R and G312A-K436R had substrate specificities, kinetic parameters and pH optima similar to those of the wild-type enzyme; however, the enzymes with substitutions K436R and G312A-K436R, had an optimal temperature of 45 °C instead of the 40 °C for the wild-type enzyme. The half-life time at 55 °C increased from 15 to 25. min for the double mutant. Molecular modeling suggests that the increase in thermostability was due to new hydrophobic interactions and the formation of a salt bridge and hydrogen bond in the G312A and K436R variants, respectively. The double mutant could be a potential candidate for application in the bread industry. © 2010 Elsevier Ltd.
Authors & Co-Authors
Mabrouk, Sameh Ben
Tunisia, Sfax
Centre de Biotechnologie de Sfax
Aghajari, Nushin
France, Lyon
Biosciences Gerland-lyon Sud
Ben Ali, Mamdouh
Tunisia, Sfax
Centre de Biotechnologie de Sfax
Messaoud, Ezzedine Ben
Tunisia, Sfax
Centre de Biotechnologie de Sfax
Juy, Michel
France, Lyon
Biosciences Gerland-lyon Sud
Haser, Richard
France, Lyon
Biosciences Gerland-lyon Sud
Bejar, S.
Tunisia, Sfax
Centre de Biotechnologie de Sfax
Statistics
Citations: 34
Authors: 7
Affiliations: 2
Identifiers
Doi:
10.1016/j.biortech.2010.08.082
ISSN:
09608524